Pinealectomy causes glucose intolerance and decreases adipose cell responsiveness to insulin in rats

1998 ◽  
Vol 275 (6) ◽  
pp. E934-E941 ◽  
Author(s):  
Fabio B. Lima ◽  
Ubiratan F. Machado ◽  
Ione Bartol ◽  
Patricia M. Seraphim ◽  
Doris H. Sumida ◽  
...  

Although the pineal gland influences several physiological systems, only a few studies have investigated its role in the intermediary metabolism. In the present study, male Wistar rats, pinealectomized or sham-operated 6 wk before the experiment, were submitted to both intravenous glucose tolerance tests (IVGTT) and insulin binding as well as glucose transport assays in isolated adipocytes. The insulin receptor tyrosine kinase activity was assessed in liver and muscle. The insulin secretory response during the IVGTT was impaired, particularly in the afternoon, and the glucose transport responsiveness was 33% lower in pinealectomized rats. However, no difference was observed in the insulin receptor number of adipocytes between groups as well as in insulin-stimulated tyrosine kinase activity, indicating that the initial steps in the insulin signaling were well conserved. Conversely, a 40% reduction in adipose tissue GLUT-4 content was detected. In conclusion, pinealectomy is responsible for both impaired insulin secretion and action, emphasizing the influence of the pineal gland on glucose metabolism.

1991 ◽  
Vol 260 (1) ◽  
pp. E1-E7 ◽  
Author(s):  
S. Azhar ◽  
J. C. Butte ◽  
R. F. Santos ◽  
C. E. Mondon ◽  
G. M. Reaven

We have examined insulin binding, autophosphorylation, and tyrosine kinase activity in detergent-solubilized and wheat germ agglutinin-purified insulin receptor preparations from four rat muscles of different fiber composition (i.e., tensor fascia latae, soleus, vastus intermedius, and plantaris). Insulin binding activity was similar in three of the four muscles but lower in tensor fascia latae. No significant differences were noted in the affinity of insulin for its receptor from various muscle types. Insulin receptor tyrosine kinase activity measured in the absence (basal) and presence of insulin (0.3-300 nM) was comparable in all muscle types (normalized to the amount of insulin bound). Insulin sensitivity, measured as the dose of insulin required for half-maximal activation of kinase activity, was also similar in all muscle types. Likewise, incubation of receptor preparations with [gamma-32P]ATP, Mn2+, and insulin (0.25-100 nM) resulted in a dose-dependent autophosphorylation of the beta-subunit (relative molecular weight approximately 95 kDa) with similar kinetics in all muscle types. In conclusion, these results show that the functional behavior of the insulin receptor autophosphorylation-kinase system (in vitro) is not changed by alterations in muscle fiber composition, indicating that differences in insulin sensitivity between different skeletal muscle types is probably not due to modulation of the insulin receptor phosphorylation system.


Diabetologia ◽  
1986 ◽  
Vol 29 (11) ◽  
pp. 798-801 ◽  
Author(s):  
D. B. Jacobs ◽  
G. R. Hayes ◽  
J. A. Truglia ◽  
D. H. Lockwood

1989 ◽  
Vol 29 (6) ◽  
pp. 653-661 ◽  
Author(s):  
R. Ballotti ◽  
Y. Le Marchand-Brustel ◽  
S. Gammeltoft ◽  
E. Van Obberghen

1998 ◽  
Vol 273 (34) ◽  
pp. 22007-22013 ◽  
Author(s):  
Jean-Olivier Contreres ◽  
Robert Faure ◽  
Gerardo Baquiran ◽  
John J. Bergeron ◽  
Barry I. Posner

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